1.14.13.195: L-ornithine N5-monooxygenase (NADPH)
This is an abbreviated version!
For detailed information about L-ornithine N5-monooxygenase (NADPH), go to the full flat file.
Word Map on EC 1.14.13.195
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1.14.13.195
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flavin
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fumigatus
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aspergillus
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flavin-dependent
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pyoverdine
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nadp+
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c4a-hydroperoxyflavin
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hydroxamate
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hydroxamate-containing
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flavin-containing
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non-ribosomal
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half-reaction
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n-hydroxylating
- 1.14.13.195
- flavin
- fumigatus
- aspergillus
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flavin-dependent
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pyoverdine
- nadp+
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c4a-hydroperoxyflavin
- hydroxamate
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hydroxamate-containing
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flavin-containing
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non-ribosomal
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half-reaction
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n-hydroxylating
Reaction
Synonyms
Af-OMO, CchB, flavin-dependent monooxygenase, L-Orn N5-oxygenase, L-ornithine N5-hydroxylase, L-ornithine-Ndelta-oxygenase, monooxygenase EtcB, omega-amino acid monooxygenase, ornithine hydroxylase, ornithine N5-monooxygenase, PsbA, PvdA, SidA, siderophore A
ECTree
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General Information
General Information on EC 1.14.13.195 - L-ornithine N5-monooxygenase (NADPH)
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metabolism
physiological function
additional information
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the enzyme catalyzes the first committed step in hydroxamate siderophore biosynthesis, e.g. N',N'',N'''-triacetylfusarinine C, i.e. TAF, and ferricrocin, which are essential for cell growth, overview
metabolism
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the enzyme catalyzes the initial step of the biosynthesis of siderophore pyoverdin
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L-ornithiine N5-oxygenase is indispensable for deferriderrichrysin biosynthesis
physiological function
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the enzyme catalyzes the first committed step in hydroxamate siderophore biosynthesis, e.g. N',N'',N'''-triacetylfusarinine C, i.e. TAF, and ferricrocin, which are essential for cell growth, overview. The enzymeis required for secretion of the siderophores and for the virulence of the organism in mice
physiological function
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the enzyme is involved in pyoverdine siderophore biosynthesis, pyoverdine is required for acquiration of the essential iron from the host
physiological function
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the enzyme is involved in the siderophore system, essential for viability, overview
physiological function
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the enzyme is required for synthesis of the nonproteinogenic amino acids N5-hydroxyornithine and N5-hydroxyformylornithine, that are required for iron assembly by the organism
physiological function
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the enzyme is required for synthesis of the nonproteinogenic amino acids N5-hydroxyornithine and N5-hydroxyformylornithine, that are required for iron assembly by the organism
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residue Asn323 interacts with the enzyme and also interacts with NADPH by forming a hydrogen bond with the nicotinamide ribose, residue K107 is important for catalytic activity. Asn323 thus facilitates ornithine binding at the expense of hindering flavin reduction
additional information
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residue Asn323 interacts with the enzyme and also interacts with NADPH by forming a hydrogen bond with the nicotinamide ribose, residue K107 is important for catalytic activity. Asn323 thus facilitates ornithine binding at the expense of hindering flavin reduction